Antimicrobial potentials of some selected microorganisms associated with supernatant solution of fermented maize mash Omidun

2012 ◽  
Vol 6 (19) ◽  
Author(s):  
Falana M. B.
Keyword(s):  
Supernatant Solution

Immunological Evidence for Prothrombin in Human Platelets

1986 ◽  
Vol 55 (02) ◽  
pp. 268-270
Author(s):  
R J Alexander
Keyword(s):  
Electrophoretic Mobility ◽  
Platelet Activation ◽  
Double Diffusion ◽  
Human Platelets ◽  
Secreted Proteins ◽  
Platelet Surface ◽  
Activated Platelets ◽  
Similar Protein ◽  
Diffusion Assay ◽  
Supernatant Solution

SummaryAn attempt was made to isolate from plasma the platelet surface substrate for thrombin, glycoprotein V (GPV), because a GPV antigen was reported to be present in plasma (3). Plasma fractionation based on procedures for purification of GPV from platelets revealed a thrombin-sensitive protein with appropriate electrophoretic mobility. The protein was purified; an antiserum against it i) reacted with detergent-solubilized platelet proteins or secreted proteins in a double diffusion assay, ii) adsorbed a protein from the supernatant solution of activated platelets, and iii) inhibited thrombin-induced platelet activation, but the antiserum did not adsorb labeled GPV. The purified protein was immunochemically related to prothrombin rather than to GPV. Other antibodies against prothrombin were also able to adsorb a protein from platelets. It is concluded that 1) plasma does not contain appreciable amounts of GPV, and 2) platelets contain prothrombin or an immunochemically similar protein.

Dissolution of Fish Muscle Homogenates by Lysolecithin

1968 ◽  
Vol 25 (10) ◽  
pp. 2157-2164
Author(s):  
R. E. E. Jonas
Keyword(s):  
Skeletal Muscle ◽  
Rainbow Trout ◽  
Snake Venom ◽  
Incubation Medium ◽  
Fish Muscle ◽  
N Content ◽  
Snake Venom Phospholipase ◽  
Solubilizing Activity ◽  
Supernatant Solution ◽  
Muscle Homogenate

On incubating skeletal muscle homogenates from rainbow trout with lysolecithin (LL) and comparing them with homogenates of the same muscle without added LL, and after centrifuging the mixtures, it was found that the N content of the supernatant solution of the homogenate containing LL was about 20% higher than that of the homogenate without LL. Increases close to maximum in N content of the supernatant solution were found to occur at a concentration of about 4 mg LL per ml of incubation medium containing 100 mg muscle in 3.0 ml of 0.9% NaCl at a pH of 6.0–8.0 and at about 35 C for a period of 1 hr. Snake venom phospholipase A added to muscle homogenate showed no solubilizing activity and α-tocopherol acetate and cortisol showed irregular stimulation. It was concluded that LL exerts a solubilizing action on fish muscle homogenates.

Enzyme Immunoassay for Screening Sulfamethazine Residues in Swine Blood

1985 ◽  
Vol 68 (2) ◽  
pp. 172-174 ◽  
Author(s):  
James R Fleeker ◽  
Leslie J Lovett
Keyword(s):  
Enzyme Immunoassay ◽  
Perchloric Acid ◽  
Labeled Compounds ◽  
Fluorogenic Substrate ◽  
Reverse Phase ◽  
Relative Response ◽  
Molar Equivalent ◽  
Supernatant Solution

Abstract An enzyme immunoassay (EIA) was developed to screen for residues of sulfamethazine (SMT) and its metabolites in swine blood. Swine blood vas treated with perchloric acid and centrifuged. The supernatant solution was neutralized with K2HP04, centrifuged, and applied to a reverse phase Cg cartridge. The analytes were eluted with methanol- water (2 + 3), and the eluate was diluted and assayed. Average recoveries, using 14C-labeled compounds, were 73, 72, 61, and 62% for SMT, W4-glucosyISMT, iV4-acetylSMT, and W4-desaminoSMT, respectively. Tubes coated with antibody were incubated with the eluate and an SMT-P-galactosidase conjugate. Bound enzyme was detected with fluorogenic substrate. When blood was fortified with 0.1 ppm SMT or a molar equivalent of metabolite, the average relative response of the EIA was 100%, control blood; 61%, SMT; 66%, glucosylSMT; 60%, acetylSMT; and 77% desaminoSMT.

scholarly journals Protein disulfide isomerase activity is released by activated platelets

Blood ◽  
1992 ◽  
Vol 79 (9) ◽  
pp. 2226-2228 ◽  
Author(s):  
K Chen ◽  
Y Lin ◽  
TC Detwiler
Keyword(s):  
Disulfide Bonds ◽  
Protein Disulfide Isomerase ◽  
Ph Dependence ◽  
Gel Filtration ◽  
Disulfide Isomerase ◽  
Isomerase Activity ◽  
Activated Platelets ◽  
Protein Disulfide ◽  
Supernatant Solution ◽  
Disulfide Isomerase Activity

Abstract The release of protein disulfide isomerase by activated platelets was hypothesized on the basis of reported intermolecular and intramolecular thiol-disulfide exchange and disulfide reduction involving released thrombospondin in the supernatant solution of activated platelets (Danishefsky, Alexander, Detwiler: Biochemistry, 23:4984, 1984; Speziale, Detwiler: J Biol Chem, 265:17859, 1990; Speziale, Detwiler: Arch Biochem Biophys 286:546, 1991). Protein disulfide isomerase activity, measured by catalysis of the renaturation of ribonuclease inactivated by randomization of disulfide bonds, was detected in the supernatant solution after platelet activation. The activity was inhibited by peptides known to inhibit protein disulfide isomerase; the peptides also inhibited formation of disulfide-linked thrombospondin- thrombin complexes. The reaction catalyzed by the supernatant solution showed a pH dependence distinct from that of the uncatalyzed reaction. The activity was excluded by a 50-Kd dialysis membrane, and it was eluted in the void volume of a gel-filtration column, indicating that it was associated with a macromolecule. The activity was not removed by centrifugation at 100,000 g for 150 minutes indicating that it was not associated with membrane microvesicles. Possible functions for the release of protein disulfide isomerase by activated platelets are discussed.

THE OXIDATION OF SUCCINATE IN EXTRACTS OF XANTHOMONAS PHASEOLI

1960 ◽  
Vol 38 (1) ◽  
pp. 481-492
Author(s):  
N. B. Madsen
Keyword(s):  
Electron Transport ◽  
Electron Transport Chain ◽  
Intact Cell ◽  
Succinic Dehydrogenase ◽  
Order Reaction ◽  
First Order ◽  
Transport Chain ◽  
Particulate Form ◽  
Supernatant Solution ◽  
Clear Supernatant

Succinoxidase and succinic dehydrogenase were found in cell-free extracts of Xanthomonas phaseoli, obtained by sonic oscillation, and remained largely in the supernatant solution after ultracentrifugation. The effect of time of exposure of the cells to sonic oscillation on cell breakage was found to follow first order reaction kinetics, as was the "solubilization" of succinic dehydrogenase and succinoxidase. It appears that the two enzymatic activities are released from the cell in a particulate form which is further fragmented on continued treatment in the sonic oscillator.The clear supernatant solution obtained after ultracentrifugation of the cell-free extract was found to contain those members of the electron transport chain which had previously been found in the intact cell, namely, flavoprotein and cytochromes b1, a1, and a2. These substances could be reduced by the addition of succinate. Malonate prevented this reduction. The effects of various inhibitors on the succinoxidase system and on succinic dehydrogenase are presented and discussed in relation to the operation of the electron transport chain in the oxidation of succinate by this organism.

Room temperature conversion of X0.3V2O5· nH2O phase into X2V6O16· nH2O phase Influence of the nature of the cation X+

2004 ◽  
Vol 848 ◽  
Author(s):  
Olivier Durupthy ◽  
Saïd Es-salhi ◽  
Nathalie Steunou ◽  
Thibaud Coradin ◽  
Jacques Livage
Keyword(s):  
Vanadium Oxide ◽  
Room Temperature ◽  
Interlayer Space ◽  
Water Molecules ◽  
X Ray Diffraction ◽  
X Ray ◽  
Oxide Phases ◽  
New Phase ◽  
Supernatant Solution ◽  
Scanning Electron

ABSTRACTVarious cations (Li+, Na+, K+, NH4+, Cs+, Mg2+, Ca2+, Ba2+) were introduced during the formation of a V2O5. nH2O gel. Cation intercalated Xy V2O5. nH2O (y = 0.3 for X = Li+, Na+, K+, NH4+ or y = 0.15 for Mg2+, Ca2+, Ba2+) were first obtained at room temperature but some of them evolve upon ageing into a new phase: XV3O8. nH2O for X = Na+, K+, NH4+ and Cs+ or XV6O16. nH2O for X = Mg2+, Ca2+, Ba2+. All the vanadium oxide phases were characterized by X-ray diffraction (XRD), scanning electron microscopy (SEM) and infrared spectroscopy (IR); the supernatant solutions were analysed by 51V NMR spectroscopy. These vanadium oxide phases exhibit a layered structure with cations and water molecules intercalated within the interlayer space. The formation of the different phases depends mainly on the pH of the supernatant solution and on the nature of the cation.

Glycerol ester hydrolase, lipase, of Myxococcus xanthus FB

1974 ◽  
Vol 20 (4) ◽  
pp. 611-615 ◽  
Author(s):  
Terje Sørhaug
Keyword(s):  
Myxococcus Xanthus ◽  
Culture Fluid ◽  
Maximal Activity ◽  
Active Principle ◽  
Ester Hydrolase ◽  
Glycerol Ester ◽  
Culture Growth ◽  
Stat Method ◽  
The Individual ◽  
Supernatant Solution

Glycerol ester hydrolase (EC. 3.1.1.3.), lipase, in liquid cultures of Myxococcus xanthus FB released up to 200–300 neq of fatty acids per milliliter per minute. Activity was assayed by the pH-stat method. Cells alone gave 0–14% and culture growth liquor alone 0–48% of the activity of a corresponding whole culture sample. Combinations when ranked according to their levels of activity in most cases followed in this order: culture direct, addition of cells to the corresponding supernatant solution during assay, recombination of the culture fluid with the corresponding cells, and the sum of the individual activities of cells and supernatant solution. Maximal activity with tributyrin as substrate was obtained at 25C and pH 8.3. Tricaprylin was the triglyceride most rapidly hydrolyzed. The active principle did not respond as a lipoprotein lipase when judged from its behavior with effectors of these enzymes.

scholarly journals Study of Adsorption from Dilute Aqueous Solutions on to Activated Carbon. Part 2. Some Exotic Adsorption Isotherms

1996 ◽  
Vol 13 (5) ◽  
pp. 341-354
Author(s):  
R. Mészáros ◽  
M. Nagy ◽  
G. Veress
Keyword(s):  
Activated Carbon ◽  
Adsorption Isotherms ◽  
Equilibrium Concentration ◽  
Model Description ◽  
Adsorption Data ◽  
Dilute Aqueous Solution ◽  
Dilute Aqueous Solutions ◽  
Error Terms ◽  
Concentration Curves ◽  
Supernatant Solution

Adsorption isotherms for the adsorption of 1-propanol and 2-propanol from dilute aqueous solution on to two types of activated carbon were presented at fixed different initial concentrations. The confidence limits for the specific excess relative to these fixed initial concentrations were also given. The high precision calculation of these error terms was based on the model description of the equilibrium concentration versus sorbent concentration curves discussed previously. The Dubinin–Radushkevich representation of the adsorption data was presented and tested for the same adsorption data. It appears that in some cases the adsorbed amount as expressed by the specific excess depends not only on the equilibrium concentration of the supernatant solution but also on the initial concentration and sorbent concentration. The so-called characteristic isotherms were also calculated in order to compare the various adsorption systems.

scholarly journals ACETYL DISULFIDE, (CH3COS)2, AND BIS-(THIOACETOXY) AURATE (I) COMPLEX, Au(CH3COS)2–, HISTOCHEMICAL SUBSTRATES OF UNUSUAL PROPERTIES WITH ACETYLCHOLINESTERASE

1968 ◽  
Vol 16 (12) ◽  
pp. 754-764 ◽  
Author(s):  
GEORGE B. KOELLE ◽  
RICHARD DAVIS ◽  
MARTINA DEVLIN
Keyword(s):  
Metal Ion ◽  
Histochemical Staining ◽  
Histochemical Reaction ◽  
Black Precipitate ◽  
Spontaneous Hydrolysis ◽  
Sigmoid Curve ◽  
Fine Localization ◽  
Thiolacetic Acid ◽  
Bell Shaped Curve ◽  
Supernatant Solution

The histochemical reaction for acetylcholinesterase (AChE) employing acetyl disulfide ([CH3COS]2, or AcDiS) as substrate and 0.006 M Pb(NO3)2 as capturing agent was characterized by (1) a sigmoid curve for velocity of hydrolysis versus substrate concentration and (2) a red precipitate (presumably [CH3COSS]2Pb) at sites of AChE at the motor endplates (MEP's) and (from spontaneous hydrolysis) in the supernatant solution. With the addition of 0.03 M thiolacetic acid (TA) to the incubation medium, which by itself produced little or no histochemical staining, the foregoing characteristics were changed to (1) a bell-shaped curve, with the peak at 0.003 M AcDiS, and (2) a black precipitate (presumably PbS) at the MEP's and in the supernatant solution; in addition, the velocity of hydrolysis was increased approximately 100-fold. Comparable differences were obtained with AcDiS as substrate when using ionic Au+ or Au(S2O3)2–3 as the capturing agent. Results are explained on the basis that in the absence of free heavy metal ion ( i.e., with the Pb[TA]2 or Au[S2O3]2–3 complex), AcDiS combines with AChE at both the anionic and esteratic sites, whereas, in the presence of Pb2+ or Au+, attachment of the substrate occurs only at the esteratic site of the enzyme. Results similar to the former type were obtained when the bis-(thioacetoxy) aurate (I) complex (Au[CH3COS]2– or Au[TA]2– served as both substrate and capturing agent. With both the AcDiS-Au(S2O3)2–3 and Au (TA)2– methods, extremely fine localization of AChE was obtained at the MEP's by electron microscopy.

Sign in / Sign up

Export Citation Format

Share Document